Plasmodium falciparum mitochondria import tRNAs along with {Soft hyphen}{Soft hyphen}{Soft hyphen}{Soft hyphen}an active phenylalanyl-tRNA synthetase{Soft hyphen}{Soft hyphen}{Soft hyphen}{Soft hyphen}

Plasmodium falciparum protein translation enzymes aminoacyl-tRNA synthetases (aaRSs) are an emergent family of drug targets. The aaRS ensemble catalyzes transfer of amino acids to cognate transfer RNAs (tRNAs), thus providing charged tRNAs for ribosomal consumption. P. falciparum proteome expression relies on total of 36 aaRSs for the three translationally independent compartments of cytoplasm, apicoplast and mitochondria. Here we show that of this set of 36, a single genomic copy of phenylalanyl-tRNA synthetase (mFRS) is targeted to the parasite mitochondria, and that mFRS gene is exclusive to malaria parasites within the apicomplexan phyla.Our protein cellular localization studies based on immunofluorescence data show that along with mFRS, P. falciparum harbors two more phenylalanine-tRNA synthetase (FRS) assemblies that are localized to its apicoplast and cytoplasm. The ‘extra’ mFRS is found in mitochondria during all asexual blood stage parasites and is competent in aminoacylation activity. We further show that the parasite mitochondria import tRNAs from the cytoplasmic pool of tRNAs. Hence, drug targeting of FRSs presents a unique opportunity to potentially stall protein production in all three parasite translational compartments concomitantly.
Source: BJ Cell - Category: Biochemistry Authors: Tags: BJ Cell Source Type: research